Abstract
Gene duplication and transposition are known to be involved in the mechanism of antigenic variation in Trypanosoma brucei1–3. However, the structure of the antigens in question—the variant surface glycoproteins (VSGs)—is poorly defined. Limited sequencing data show extensive variation between the N-terminal amino acid sequences of different VSGs4,5, although serological studies indicate common antigenic determinants in the C-terminal portion (refs 6, 7 and N. Van Meirvenne, personal communication). More recently, the existence of a C-terminal hydrophobic tail, which is absent from the isolated glycoprotein, was reported8. We have now compared the messenger RNA sequences corresponding to the C-terminal 115 amino acids of two serologically different variants belonging to the same serodeme and report a 35% lack of homology (52% of amino acid positions). However, there is a large homologous area of 33 amino acids making up the C-terminus, which includes the 23-amino acid hydrophobic tail. Our data indicate that this extension is a universal feature in T. brucei VSGs. In addition, comparison of two isotypes (serologically similar VSGs) belonging to different serodemes showed almost complete nucleotide homology in the coding sequence of the C-terminal 115 amino acids.
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Matthyssens, G., Michiels, F., Hamers, R. et al. Two variant surface glycoproteins of Trypanosoma brucei have a conserved C-terminus. Nature 293, 230–233 (1981). https://doi.org/10.1038/293230a0
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DOI: https://doi.org/10.1038/293230a0
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